SNX21_HUMAN
ID SNX21_HUMAN Reviewed; 373 AA.
AC Q969T3; Q5JZH5; Q5JZH6; Q5JZH7; Q8WUR6; Q9BR16;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Sorting nexin-21;
DE AltName: Full=Sorting nexin L;
DE Short=SNX-L {ECO:0000303|PubMed:12459172};
GN Name=SNX21; Synonyms=C20orf161, SNXL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Hong W.;
RT "A new member (SNX21) of the sorting nexin protein family.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=12459172; DOI=10.1016/s0006-291x(02)02695-5;
RA Zeng W., Yuan W., Wang Y., Jiao W., Zhu Y., Huang C., Li D., Li Y., Zhu C.,
RA Wu X., Liu M.;
RT "Expression of a novel member of sorting nexin gene family, SNX-L, in human
RT liver development.";
RL Biochem. Biophys. Res. Commun. 299:542-548(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Stavrides G.S., Huckle E.J., Deloukas P.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-154.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol 3-
CC phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate. May
CC be involved in several stages of intracellular trafficking.
CC {ECO:0000250|UniProtKB:Q3UR97}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q3UR97}.
CC -!- INTERACTION:
CC Q969T3-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-12142321, EBI-7116203;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q3UR97}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Early endosome membrane
CC {ECO:0000250|UniProtKB:Q3UR97}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q3UR97}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q3UR97}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q969T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969T3-2; Sequence=VSP_045048, VSP_045049;
CC Name=3;
CC IsoId=Q969T3-3; Sequence=VSP_047115;
CC -!- TISSUE SPECIFICITY: Highly expressed in fetus liver, but only weakly
CC expressed in brain, skeleton muscle, smooth muscle, and cardiac muscle,
CC kidney, and adrenal gland. {ECO:0000269|PubMed:12459172}.
CC -!- DOMAIN: The PX domain mediates specific binding to membranes enriched
CC in phosphatidylinositol 3-phosphate (PtdIns(P3)).
CC {ECO:0000250|UniProtKB:Q3UR97}.
CC -!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
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DR EMBL; AF395845; AAK73126.1; -; mRNA.
DR EMBL; AF523834; AAM77915.1; -; mRNA.
DR EMBL; AL591562; CAC39140.1; -; mRNA.
DR EMBL; AL008726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019823; AAH19823.1; -; mRNA.
DR CCDS; CCDS13376.1; -. [Q969T3-2]
DR CCDS; CCDS13377.1; -. [Q969T3-1]
DR CCDS; CCDS42883.1; -. [Q969T3-3]
DR RefSeq; NP_219489.1; NM_033421.3. [Q969T3-1]
DR RefSeq; NP_690857.1; NM_152897.2. [Q969T3-2]
DR AlphaFoldDB; Q969T3; -.
DR SMR; Q969T3; -.
DR BioGRID; 124677; 73.
DR IntAct; Q969T3; 33.
DR STRING; 9606.ENSP00000418593; -.
DR GlyGen; Q969T3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q969T3; -.
DR PhosphoSitePlus; Q969T3; -.
DR BioMuta; SNX21; -.
DR DMDM; 20140138; -.
DR EPD; Q969T3; -.
DR jPOST; Q969T3; -.
DR MassIVE; Q969T3; -.
DR MaxQB; Q969T3; -.
DR PaxDb; Q969T3; -.
DR PeptideAtlas; Q969T3; -.
DR PRIDE; Q969T3; -.
DR ProteomicsDB; 63536; -.
DR ProteomicsDB; 63537; -.
DR ProteomicsDB; 75842; -. [Q969T3-1]
DR Antibodypedia; 27775; 82 antibodies from 17 providers.
DR DNASU; 90203; -.
DR Ensembl; ENST00000342644.9; ENSP00000344586.5; ENSG00000124104.19. [Q969T3-2]
DR Ensembl; ENST00000462307.5; ENSP00000420169.1; ENSG00000124104.19. [Q969T3-3]
DR Ensembl; ENST00000491381.6; ENSP00000418593.1; ENSG00000124104.19. [Q969T3-1]
DR GeneID; 90203; -.
DR KEGG; hsa:90203; -.
DR MANE-Select; ENST00000491381.6; ENSP00000418593.1; NM_033421.4; NP_219489.1.
DR UCSC; uc002xps.2; human. [Q969T3-1]
DR CTD; 90203; -.
DR GeneCards; SNX21; -.
DR HGNC; HGNC:16154; SNX21.
DR HPA; ENSG00000124104; Low tissue specificity.
DR MIM; 619200; gene.
DR neXtProt; NX_Q969T3; -.
DR OpenTargets; ENSG00000124104; -.
DR PharmGKB; PA25703; -.
DR VEuPathDB; HostDB:ENSG00000124104; -.
DR eggNOG; KOG2101; Eukaryota.
DR GeneTree; ENSGT00530000063759; -.
DR InParanoid; Q969T3; -.
DR OMA; EAQEHCD; -.
DR OrthoDB; 1322681at2759; -.
DR PhylomeDB; Q969T3; -.
DR TreeFam; TF326807; -.
DR PathwayCommons; Q969T3; -.
DR SignaLink; Q969T3; -.
DR BioGRID-ORCS; 90203; 17 hits in 1080 CRISPR screens.
DR ChiTaRS; SNX21; human.
DR GeneWiki; SNX21; -.
DR GenomeRNAi; 90203; -.
DR Pharos; Q969T3; Tdark.
DR PRO; PR:Q969T3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q969T3; protein.
DR Bgee; ENSG00000124104; Expressed in skin of leg and 174 other tissues.
DR ExpressionAtlas; Q969T3; baseline and differential.
DR Genevisible; Q969T3; HS.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.30.1520.10; -; 1.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR039937; SNX20/SNX21.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR20939; PTHR20939; 1.
DR Pfam; PF00787; PX; 1.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF64268; SSF64268; 1.
DR PROSITE; PS50195; PX; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasmic vesicle; Endosome; Lipid-binding;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..373
FT /note="Sorting nexin-21"
FT /id="PRO_0000213870"
FT DOMAIN 129..246
FT /note="PX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00147"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T1"
FT BINDING 173
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q96L94"
FT BINDING 198
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q96L94"
FT BINDING 212
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3-phosphate)"
FT /ligand_id="ChEBI:CHEBI:58088"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T1"
FT VAR_SEQ 150..373
FT /note="LYTLAVIGPGPPDCQPAQISRRYSDFERLHRNLQRQFRGPMAAISFPRKRLR
FT RNFTAETIARRSRAFEQFLGHLQAVPELRHAPDLQDFFVLPELRRAQSLTCTGLYREAL
FT ALWANAWQLQAQLGTPSGPDRPLLTLAGLAVCHQELEDPGEARACCEKALQLLGDKSLH
FT PLLAPFLEAHVRLSWRLGLDKRQSEARLQALQEAGLTPTPPPSLKELLIKEVLD -> T
FT NLSSTPSP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047115"
FT VAR_SEQ 197..199
FT /note="RKR -> QSH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045048"
FT VAR_SEQ 200..373
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045049"
FT VARIANT 154
FT /note="A -> T (in dbSNP:rs4638862)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_052482"
SQ SEQUENCE 373 AA; 41365 MW; 83E4A752BAAEA7B5 CRC64;
MHRGTQEGAM ASRLLHRLRH ALAGDGPGEA AASPEAEQFP ESSELEDDDA EGLSSRLSGT
LSFTSAEDDE DDEDEDDEEA GPDQLPLGDG TSGEDAERSP PPDGQWGSQL LARQLQDFWK
KSRNTLAPQR LLFEVTSANV VKDPPSKYVL YTLAVIGPGP PDCQPAQISR RYSDFERLHR
NLQRQFRGPM AAISFPRKRL RRNFTAETIA RRSRAFEQFL GHLQAVPELR HAPDLQDFFV
LPELRRAQSL TCTGLYREAL ALWANAWQLQ AQLGTPSGPD RPLLTLAGLA VCHQELEDPG
EARACCEKAL QLLGDKSLHP LLAPFLEAHV RLSWRLGLDK RQSEARLQAL QEAGLTPTPP
PSLKELLIKE VLD
